Tetraethylammonium block of water flux in Aquaporin-1 channels expressed in kidney thin limbs of Henle's loop and a kidney-derived cell line.
AJ Yool, OH Brokl, TL Pannabecker, WH Dantzler… - BMC physiology, 2002 - Springer
Abstract Background Aquaporin-1 (AQP1) channels are constitutively active water channels
that allow rapid transmembrane osmotic water flux, and also serve as cyclic-GMP-gated ion …
that allow rapid transmembrane osmotic water flux, and also serve as cyclic-GMP-gated ion …
Cloned human aquaporin-1 is a cyclic GMP-gated ion channel
Aquaporin-1 (AQP1) is a member of the membrane intrinsic protein (MIP) gene family and is
known to provide pathways for water flux across cell membranes. We show here that cloned …
known to provide pathways for water flux across cell membranes. We show here that cloned …
Aquaporin-1, nothing but a water channel
SP Tsunoda, B Wiesner, D Lorenz, W Rosenthal… - Journal of Biological …, 2004 - ASBMB
Aquaporin-1 (AQP1) is a membrane channel that allows rapid water movement driven by a
transmembrane osmotic gradient. It was claimed to have a secondary function as a cyclic …
transmembrane osmotic gradient. It was claimed to have a secondary function as a cyclic …
Aquaporin-1 channel function is positively regulated by protein kinase C
W Zhang, E Zitron, M Hoömme, L Kihm… - Journal of Biological …, 2007 - ASBMB
Aquaporin-1 (AQP1) channels contribute to osmotically induced water transport in several
organs including the kidney and serosal membranes such as the peritoneum and the pleura …
organs including the kidney and serosal membranes such as the peritoneum and the pleura …
Role of multiple phosphorylation sites in the COOH-terminal tail of aquaporin-2 for water transport: evidence against channel gating
HB Moeller, N MacAulay… - American Journal of …, 2009 - journals.physiology.org
Arginine vasopressin (AVP)-regulated phosphorylation of the water channel aquaporin-2
(AQP2) at serine 256 (S256) is essential for its accumulation in the apical plasma membrane …
(AQP2) at serine 256 (S256) is essential for its accumulation in the apical plasma membrane …
Mutation of a single amino acid converts the human water channel aquaporin 5 into an anion channel
X Qin, WF Boron - American Journal of Physiology-Cell …, 2013 - journals.physiology.org
Aquaporin 6 (AQP6) is unique among mammalian AQPs in being an anion channel with
negligible water permeability. However, the point mutation Asn60Gly converts AQP6 from an …
negligible water permeability. However, the point mutation Asn60Gly converts AQP6 from an …
Ion permeation of AQP6 water channel protein: single-channel recordings after Hg2+ activation
Aquaporin-6 (AQP6) has recently been identified as an intracellular vesicle water channel
with anion permeability that is activated by low pH or HgCl 2. Here we present direct …
with anion permeability that is activated by low pH or HgCl 2. Here we present direct …
Inhibition of aquaporin-1 water permeability by tetraethylammonium: involvement of the loop E pore region
Previously, the only known blockers of water permeability through aquaporin-1 (AQP1)
water channels were mercurial reagents such as HgCl2. For AQP1, inhibition by mercury …
water channels were mercurial reagents such as HgCl2. For AQP1, inhibition by mercury …
The activity of human aquaporin 1 as a cGMP-gated cation channel is regulated by tyrosine phosphorylation in the carboxyl-terminal domain
In addition to a constitutive water channel activity, several studies suggest Aquaporin-1
(AQP1) functions as a nonselective monovalent cation channel activated by intracellular …
(AQP1) functions as a nonselective monovalent cation channel activated by intracellular …
Selectivity of the renal collecting duct water channel aquaporin-3
M Echevarría, EE Windhager, G Frindt - Journal of Biological Chemistry, 1996 - ASBMB
Aquaporin-3 (AQP3) is a water channel found in the basolateral cell membrane of principal
cells of the renal collecting tubule as well as in other epithelia. To examine the selectivity of …
cells of the renal collecting tubule as well as in other epithelia. To examine the selectivity of …